TraitMech

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heat shock response

traitmech:000205 · CLASS · PROPOSED

A stress response in which acute heat stress induces heat-shock proteins that refold or degrade denatured proteins to restore protein homeostasis.

Trait evidence (4)

  • DOI:10.1007/s12192-016-0727-z
    they transiently induce a group of genes called heat shock genes (HSGs) which code for heat shock proteins (HSPs)

    Schumann reviews heat-shock gene induction and heat-shock protein production as the bacterial response to sudden temperature rise.

  • DOI:10.1007/s12192-016-0727-z
    chaperones binding to denatured proteins and allowing refolding to their native state and ATP-dependent proteases degrading denatured proteins

    Schumann summarizes the two major functional heat-shock protein classes that clear denatured proteins.

  • DOI:10.1128/MMBR.00007-08
    The heat shock response (HSR) is classically defined as the cellular response to temperature increase

    Guisbert et al. define the E. coli heat-shock response and review the sigma-32 regulatory model.

  • DOI:10.1128/MMBR.00007-08
    The rapid upregulation of chaperones and proteases during the HSR restores an appropriate protein-folding environment in the cell

    Guisbert et al. support protein-folding homeostasis as the primary function of the E. coli sigma-32-mediated heat-shock response.

Heat-shock proteostasis restoration

Evidence-backed causal sketch linking acute heat shock to protein unfolding, heat-shock protein induction, and restored protein homeostasis.

MECHANISTIC · This graph captures the conserved proteostasis output of the heat-shock response without making the E. coli sigma-32 branch, B. subtilis HrcA/CtsR branches, or other lineage-specific heat-shock regulators universal.

Heat-shock proteostasis restoration Interactive directed graph showing evidence-backed causal relationships for heat shock response.

Edge evidence

  • acute heat shock causes heat-induced protein unfolding biolink:causes

    Acute heat shock causes protein unfolding and aggregate formation.

    • DOI:10.1007/s12192-016-0727-z A sudden heat shock results in protein unfolding leading to the formation of protein aggregates Verified against the open PMC full text; heat shock immediately destabilizes cellular proteins.
  • heat-induced protein unfolding causes heat-shock response biolink:causes

    Protein unfolding and aggregation trigger rapid, transient heat-shock protein production.

    • DOI:10.1007/s12192-016-0727-z It responds to protein unfolding, aggregation and damage by the rapid and transient production of HSPs Verified against the open PMC full text; the edge links damaged unfolded proteins to the protective heat-shock response.
  • heat-shock response positively regulates heat-shock chaperones RO:0002213

    The heat-shock response induces chaperones that refold denatured proteins.

    • DOI:10.1007/s12192-016-0727-z chaperones binding to denatured proteins and allowing refolding to their native state Verified against the open PMC full text; chaperones are a major heat-shock protein class.
  • heat-shock response positively regulates ATP-dependent proteases RO:0002213

    The heat-shock response induces ATP-dependent proteases that remove denatured proteins.

    • DOI:10.1007/s12192-016-0727-z ATP-dependent proteases degrading denatured proteins Verified against the open PMC full text; ATP-dependent proteases are a major heat-shock protein class.
  • heat-shock chaperones contributes to protein homeostasis RO:0002326

    Heat-shock chaperones help restore proteostasis by refolding denatured proteins.

    • DOI:10.1007/s12192-016-0727-z chaperones binding to denatured proteins and allowing refolding to their native state Verified against the open PMC full text; induced chaperones support refolding of denatured proteins.
  • ATP-dependent proteases contributes to protein homeostasis RO:0002326

    ATP-dependent proteases help restore proteostasis by degrading denatured proteins.

    • DOI:10.1007/s12192-016-0727-z ATP-dependent proteases degrading denatured proteins Verified against the open PMC full text; induced proteases clear denatured proteins.
  • protein homeostasis confers heat shock response METPO:2007700

    Restoration of protein-folding homeostasis realizes the heat-shock-response trait.

    • DOI:10.1128/MMBR.00007-08 restores an appropriate protein-folding environment in the cell Verified against the open PMC full text; Guisbert et al. describe proteostasis restoration as the sigma-32-mediated heat-shock response output.

Protein and taxon examples

Graph nodeProteinTaxonUniProt statusRole and evidence
heat-shock chaperones UniProtKB:P0A6Y8
Chaperone protein DnaK (dnaK) 		Escherichia coli K-12
NCBITaxon:83333 		REVIEWED
retrieved 2026-09-15 · entry v183 · sequence v2

E. coli K-12 DnaK is an Hsp70 heat-shock chaperone that binds sigma-32 in the chaperone-mediated heat-shock control branch.

  • DOI:10.1073/pnas.89.8.3516 purified sigma 32 bound to DnaK and that this complex was disrupted in the presence of ATP Liberek et al. directly support DnaK as an E. coli heat-shock chaperone that binds the sigma-32 transcription factor.
ATP-dependent proteases UniProtKB:P0AAI3
ATP-dependent zinc metalloprotease FtsH (ftsH) 		Escherichia coli K-12
NCBITaxon:83333 		REVIEWED
retrieved 2026-09-15 · entry v155 · sequence v1

E. coli K-12 FtsH is an ATP-dependent membrane metalloprotease that degrades the sigma-32 heat-shock transcription factor.

  • DOI:10.1002/j.1460-2075.1995.tb07253.x FtsH catalyzed ATP-dependent degradation of biologically active histidine-tagged sigma 32 Tomoyasu et al. directly support FtsH as the E. coli ATP-dependent protease that degrades sigma-32.

Provenance

Identifier source
TraitMech local identifier
Definition source
DOI:10.1007/s12192-016-0727-z

Parent traits (1)

Synonyms (2)

  • heat-shock response EXACT_SYNONYM · DOI:10.1007/s12192-016-0727-z
  • HSR RELATED_SYNONYM · DOI:10.1128/MMBR.00007-08

kg-microbe context

No kg-microbe node embedding matched this record in the 2026-04-25 deepwalk.

Canonical examples (2)

Organisms cited as exemplars of this trait. Taxon ids are NCBITaxon and link out to the NCBI record.

Discussions and Knowledge Gaps (1)

Open questions attached to this trait. Seeded by just knowledge-gap-scan and curated; see the corpus-wide index.

Resolve exact ontology xrefs for organism-level microbial heat shock response before adding TraitRecord xrefs.

CURATION TODO OPEN heat-shock-response-xref-gap · raised by codex · 2026-09-15

Not yet attached to a section of this record — a curator sets attaches_to (e.g. causal_graphs#some_edge) so the gap shows beside the mechanism it concerns.

GO:0009408 response to heat can ground biological-process nodes but is broader than this organism-level stress response trait. Candidate heat-shock-protein, chaperone, and ATP-dependent-protease terms describe narrower molecular machinery rather than the whole response phenotype.

Curation history

  1. · MINTED_TRAITMECH_ID · codex

    Minted heat shock response as a DOI-backed stress-response TraitRecord after a repository-wide duplicate review covering ignored and hidden files; the local METPO snapshot has only an obsolete heat shock response class and the replacement placeholder is reserved in proposals/metpo_traitmech_v82.